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Human Polyclonal SMUG1 Primary Antibody for ELISA, WB - ABIN250205
Boorstein, Cummings, Marenstein, Chan, Ma, Neubert, Brown, Teebor: Definitive identification of mammalian 5-hydroxymethyluracil DNA N-glycosylase activity as SMUG1. in The Journal of biological chemistry 2001
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Human Polyclonal SMUG1 Primary Antibody for ELISA, IHC - ABIN185204
Ma, Au, Waye: Over-expression of SUMO-1 induces the up-regulation of heterogeneous nuclear ribonucleoprotein A2/B1 isoform B1 (hnRNP A2/B1 isoform B1) and uracil DNA glycosylase (UDG) in hepG2 cells. in Cell biochemistry and function 2009
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Human Polyclonal SMUG1 Primary Antibody for ELISA, WB - ABIN565120
Doseth, Visnes, Wallenius, Ericsson, Sarno, Pettersen, Flatberg, Catterall, Slupphaug, Krokan, Kavli: Uracil-DNA glycosylase in base excision repair and adaptive immunity: species differences between man and mouse. in The Journal of biological chemistry 2011
we showed that SMUG1 efficiently prevent genomic uracil accumulation, even in the presence of UNG, and identified mutational signatures associated with combined UNG and SMUG1 deficiency.
Nonetheless, using a highly MSH2-dependent mechanism, Ung(-/-) Smug1(-/-) mice can still produce detectable levels of switched isotypes, especially IgG1
SMUG1 is the dominant glycosylase responsible for 5-hydroxymethyluracil-excision in mice as well as the major UNG-backup for U-excision.
analysis of species specific differences between mouse and humans in regulation of SMUG1 and UNG2
The structure and specificity of SMUG1 have been solved.
This analysis showed a relative increase in the expression of E2F6 in gastric adenocarcinoma with no lymph node metastasis (chi (2), P = 0.04 and OR, P = 0.08), while overexpression of RhoA and SMUG1 was found more often in the diffuse subtype of gastric adenocarcinoma as compared to the intestinal subtype.
Our study showed that c.-31A/G-SMUG1 genotypes/alleles do not have any association with the occurrence or severity of advanced type age-related macular degeneration (AMD). There was no interaction of CRP levels and SMUG1 genotypes in AMD susceptibility.
A case-control study of 801 bladder cancer patients and 801 matched controls, the associations of 167 single nucleotide polymorphisms (SNPs) from 19 genes of the BER pathway with the risk of bladder cancer; 13 SNPs in 10 Base excision repair (BER) pathway genes were significantly associated with bladder cancer risk; most significant SNP was rs2029167 in the SMUG1 gene.
Single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) deficiency is linked to aggressive breast cancer and predicts response to adjuvant therapy.
The results obtained suggest the potential role of the g.4235T>C and the c.-31A>G polymorphisms in AMD pathogenesis.
There was no difference between SMUG1 proficient and depleted cells following continuous exposure.
SMUG1 is a DKC1 interaction partner that contributes to rRNA quality control, partly by regulating 5-hydroxymethyluridine levels.
Data show that uracil-DNA glycosylases SMUG1 and UNG2 display widely different sequence preferences.
there was increased risk of breast cancer among postmenopausal women heterozygous for either SMUG1 rs2029166 or rs7296239. Among premenopausal women, the increased risk associated with SMUG1 rs2029166 was limited to those with low folate intake.
hSMUG1 is a broad specificity backup for hUNG2, the major enzyme for removal of deaminated cytosine in single strnaded DNA
This enzyme has a role in repair of 5-formyluracil and other oxidized and deaminated base lesions.
Site-directed mutagenesis was used to determine the catalytic and DNA damage-recognition mechanism of hSMUG1.
SMUG1 plays little natural role in antibody diversification.
A G44T missense mutation was found in familial colorectal cancer DNA suggesting a limited role for this gene in the devlopment of CRC.
Analysis of the catalytic and precision damage recognition mechanisms of SMUG1.
SMUG1 and UNG2 coordinate the initial steps in base excision repair of U:G mismatches by different molecular mechanisms.
proline substitution at the G63 position switches the Gme SMUG1 enzyme to an exclusive UDG as demonstrated by the uniform excision of uracil in both double-stranded and single-stranded DNA and the complete loss of XDG activity
Properties used by hSMUG1 to select damaged pyrimidines include the size and free energy of solvation of the 5-substituent but not electronic inductive properties.
This gene encodes a protein that participates in base excision repair by removing uracil from single- and double-stranded DNA. Many alternatively spliced transcript variants exist for this gene\; the full-length nature is known for some but not all of the variants.
single-strand-selective monofunctional uracil-DNA glycosylase 1
, single-strand selective monofunctional uracil DNA glycosylase
, single-strand selective monofunctional uracil-DNA glycosylase